Thermal stability and unfolding pathways of Sso7d and its mutant F31A: insight from molecular dynamics simulation.

Abstract excerpt

The thermo-stability and unfolding behaviors of a small hyperthermophilic protein Sso7d as well as its single-point mutation F31A are studied by molecular dynamics simulation at temperatures of 300 K, 371 K and 500 K. Simulations at 300 K show that the F31A mutant displays a much larger flexibility than the wild type, which implies that the mutation obviously decreases the protein's stability. In the simulations...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Archaeal Proteins
• Share to Hydrogen Bonding